WGU C785 BIOCHEMISTRY EXAM
What is the basic structure of an amino acid? What do amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C),
they look like? and variable group
How do you identify the 3 different types of side chains: Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH,
non-polar/hydrophobic, polar, and charged? SH, or NH. Charged - end with a charge
what kinds of bonds do each of the 3 different types of ionic, hydrophobic/non-polar, charged
side chains make?
What are the 4 levels of protein structure? Primary - linear structure, Secondary - Folded into helix or pleated sheet caused
by hydrogen bonding, tertiary - 3D structure caused by side chain interactions,
quaternary - 1+ amino acid chains combine = multiple subunits MUST have 1+
subunit
What enviormental change breaks each type of bond? hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen -
temperature, change in pH, disulfide - reducing agents
what type of amino acid side chain leads to protein hydrophobic bonds
aggregration?
how do environmental changes affect protein folding? Extreme temp can cause hydrogen bonds to break apart = malformation of
protein folding
how do mutations affect protein structure? Can cause structure to change. Protein loses form = loses function. May form a
different protein.
What is an electron? Negatively charged atom on outer ring for bonding
What is energy: Power derived fro chemical interaction
what are covalent bonds? chemical bond, atoms share 1+ valence electrons
what is an ionic bond? bond between positive and negative
what is a hydrogen bond? weak bond between positive and negative
with an amino? piece of amino acid, NH2 or NH3
what is a carboyxl? piece of amino acid, COO or COOH
What is hydrophobic? Doesn't like water, end with CH
, WGU C785 BIOCHEMISTRY EXAM
what is hydrophilic? Water Lovering, end with OH, NH, or SH
what is disulfide bond? strongest bond between reduction agents, formed between SH's.
what are zwitterions? amino with positive and negative charges = overall charge of zero
what is a polypeptide polymer of amino acids
What is dehydration synthesis? Process of forming peptide bonds
what is hydrolysis? adding water to destroy bonds
what is an alpha helix? twisted secondary structure, formed by hydrogen bonds
what is a beta sheet? folded second structure shape, formed by hydrogen bonds
what is denaturation? loss of shape duet o interruption of chemical bonds; occurs via extreme salt,
temp, pH
what is aggregation? clumping of inner or outer cellular proteins caused by misfolded proteins leading
to diseases such as Alzheimers, ALS, Parkinson's
how do enzymes catalyze reactions? bind with substrates to decrease activation energy required and decrease
reaction rate
how do enzymes affect reaction rate and activation decrease activation energy and decrease reaction rate
energy?
what are the 4 steps of the enzymatic cycle? enzyme recognizes substrate, substrate attracts the enzyme; enzyme-substrate
complex is formed; enzyme-product complex formed; product is released,
enzyme recycled
how do environmental changes affect enzymes? High heat, pH change, high salt concentration, and reducing agents can cause
an enzyme to lose its form/lose function
what is a competitive inhibitor? Mimics substrate and takes its place on the active binding site
what is a noncompetitive inhibitor? Binds to allosteric site causing active site to change shape = preventing
substrate from binding with enzyme
, WGU C785 BIOCHEMISTRY EXAM
what molecules increase/build up or decrease given a Inhibitor would cause a build up for product B, decrease product C. Enzyme 3
specific inhibitor? A -> (enzyme 1) -> B -> (enzyme 2) -> and product D would not be created.
C -> (enzyme 3) -> D. Pretend Enzyme 2 is inhibited.
what is substrate? the substance on which an enzyme acts
what is a product? result of a reaction
what is an intermediate? products produced in an enzyme pathway before final product
what is an active site? location where substrate binds with enzyme
what is enzyme specificity? Enzymes bind with certain substrate or type of substrate to create a certain
reaction
what is induced fit? Enzyme changes shape in enzyme-substrate complex to facilitate formation of
enzyme-product complex
what is kinase? Enzyme, adds phosphate group via phosphorlation
what is phosphatase? enzyme, removes phosphate group via dephosphorylation
with is an allosteric site? secondary site on an enzyme an inhibitor binds to via non-competitive inhibition
what is competitive inhibition? enzyme substrate and inhibitor complex compete to bind with enzyme's active
site. no product formed when inhibitor binds with enzyme.
what is non-competitive inhibition? inhibitor binds to allosteric site, not active site. Changes shape of active site,
preventing substrate from binding and making product
what is feedback inhibition? End product sends feedback to beginning of enzyme pathway inhibiting 1st
enzyme via noncompetitive inhibition
what nucleotides/bases are used in DNA? what are their C - cytosine, G - guanine, A - adenine, T - thyamine
abbreviations/full names?
what nucleotides/bases are used in RNA? C - cytosine, G - guanine, U - uracil, A - adenine
which nucleotides base-pair together in DNA? T-A, G-C
What is the basic structure of an amino acid? What do amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C),
they look like? and variable group
How do you identify the 3 different types of side chains: Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH,
non-polar/hydrophobic, polar, and charged? SH, or NH. Charged - end with a charge
what kinds of bonds do each of the 3 different types of ionic, hydrophobic/non-polar, charged
side chains make?
What are the 4 levels of protein structure? Primary - linear structure, Secondary - Folded into helix or pleated sheet caused
by hydrogen bonding, tertiary - 3D structure caused by side chain interactions,
quaternary - 1+ amino acid chains combine = multiple subunits MUST have 1+
subunit
What enviormental change breaks each type of bond? hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen -
temperature, change in pH, disulfide - reducing agents
what type of amino acid side chain leads to protein hydrophobic bonds
aggregration?
how do environmental changes affect protein folding? Extreme temp can cause hydrogen bonds to break apart = malformation of
protein folding
how do mutations affect protein structure? Can cause structure to change. Protein loses form = loses function. May form a
different protein.
What is an electron? Negatively charged atom on outer ring for bonding
What is energy: Power derived fro chemical interaction
what are covalent bonds? chemical bond, atoms share 1+ valence electrons
what is an ionic bond? bond between positive and negative
what is a hydrogen bond? weak bond between positive and negative
with an amino? piece of amino acid, NH2 or NH3
what is a carboyxl? piece of amino acid, COO or COOH
What is hydrophobic? Doesn't like water, end with CH
, WGU C785 BIOCHEMISTRY EXAM
what is hydrophilic? Water Lovering, end with OH, NH, or SH
what is disulfide bond? strongest bond between reduction agents, formed between SH's.
what are zwitterions? amino with positive and negative charges = overall charge of zero
what is a polypeptide polymer of amino acids
What is dehydration synthesis? Process of forming peptide bonds
what is hydrolysis? adding water to destroy bonds
what is an alpha helix? twisted secondary structure, formed by hydrogen bonds
what is a beta sheet? folded second structure shape, formed by hydrogen bonds
what is denaturation? loss of shape duet o interruption of chemical bonds; occurs via extreme salt,
temp, pH
what is aggregation? clumping of inner or outer cellular proteins caused by misfolded proteins leading
to diseases such as Alzheimers, ALS, Parkinson's
how do enzymes catalyze reactions? bind with substrates to decrease activation energy required and decrease
reaction rate
how do enzymes affect reaction rate and activation decrease activation energy and decrease reaction rate
energy?
what are the 4 steps of the enzymatic cycle? enzyme recognizes substrate, substrate attracts the enzyme; enzyme-substrate
complex is formed; enzyme-product complex formed; product is released,
enzyme recycled
how do environmental changes affect enzymes? High heat, pH change, high salt concentration, and reducing agents can cause
an enzyme to lose its form/lose function
what is a competitive inhibitor? Mimics substrate and takes its place on the active binding site
what is a noncompetitive inhibitor? Binds to allosteric site causing active site to change shape = preventing
substrate from binding with enzyme
, WGU C785 BIOCHEMISTRY EXAM
what molecules increase/build up or decrease given a Inhibitor would cause a build up for product B, decrease product C. Enzyme 3
specific inhibitor? A -> (enzyme 1) -> B -> (enzyme 2) -> and product D would not be created.
C -> (enzyme 3) -> D. Pretend Enzyme 2 is inhibited.
what is substrate? the substance on which an enzyme acts
what is a product? result of a reaction
what is an intermediate? products produced in an enzyme pathway before final product
what is an active site? location where substrate binds with enzyme
what is enzyme specificity? Enzymes bind with certain substrate or type of substrate to create a certain
reaction
what is induced fit? Enzyme changes shape in enzyme-substrate complex to facilitate formation of
enzyme-product complex
what is kinase? Enzyme, adds phosphate group via phosphorlation
what is phosphatase? enzyme, removes phosphate group via dephosphorylation
with is an allosteric site? secondary site on an enzyme an inhibitor binds to via non-competitive inhibition
what is competitive inhibition? enzyme substrate and inhibitor complex compete to bind with enzyme's active
site. no product formed when inhibitor binds with enzyme.
what is non-competitive inhibition? inhibitor binds to allosteric site, not active site. Changes shape of active site,
preventing substrate from binding and making product
what is feedback inhibition? End product sends feedback to beginning of enzyme pathway inhibiting 1st
enzyme via noncompetitive inhibition
what nucleotides/bases are used in DNA? what are their C - cytosine, G - guanine, A - adenine, T - thyamine
abbreviations/full names?
what nucleotides/bases are used in RNA? C - cytosine, G - guanine, U - uracil, A - adenine
which nucleotides base-pair together in DNA? T-A, G-C
